Characterization of an Alkaline Alginate Lyase with pH-Stable and Thermo-Tolerance Property
| Autor: | Xuehong Chen, Yining Ren, Yantao Han, Ruyong Yao, Yu Zhou, Xiaolin Bi, Yanan Wang, Shangyong Li, Qi Han |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
pH-stability
Aquatic Organisms Polysaccharide-Lyases Pharmaceutical Science Initial activity medicine.disease_cause Article Alginate lyase 03 medical and health sciences Drug Discovery Enzyme Stability medicine Escherichia coli Vibrio sp. SY01 Pharmacology Toxicology and Pharmaceutics (miscellaneous) lcsh:QH301-705.5 030304 developmental biology Vibrio chemistry.chemical_classification 0303 health sciences biology 030306 microbiology Chemistry Temperature Hydrogen-Ion Concentration Thermo-tolerant biology.organism_classification Recombinant Proteins Enzyme Biochemistry lcsh:Biology (General) Specific activity Endo-manner Bacteria |
| Zdroj: | Marine Drugs, Vol 17, Iss 5, p 308 (2019) Marine Drugs Volume 17 Issue 5 |
| ISSN: | 1660-3397 |
| Popis: | Alginate oligosaccharides (AOS) show versatile bioactivities. Although various alginate lyases have been characterized, enzymes with special characteristics are still rare. In this study, a polysaccharide lyase family 7 (PL7) alginate lyase-encoding gene, aly08, was cloned from the marine bacterium Vibrio sp. SY01 and expressed in Escherichia coli. The purified alginate lyase Aly08, with a molecular weight of 35 kDa, showed a specific activity of 841 U/mg at its optimal pH (pH 8.35) and temperature (45 ° C). Aly08 showed good pH-stability, as it remained more than 80% of its initial activity in a wide pH range (4.0&ndash 10.0). Aly08 was also a thermo-tolerant enzyme that recovered 70.8% of its initial activity following heat shock treatment for 5 min. This study also demonstrated that Aly08 is a polyG-preferred enzyme. Furthermore, Aly08 degraded alginates into disaccharides and trisaccharides in an endo-manner. Its thermo-tolerance and pH-stable properties make Aly08 a good candidate for further applications. |
| Databáze: | OpenAIRE |
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